1chm

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{{STRUCTURE_1chm| PDB=1chm | SCENE= }}
{{STRUCTURE_1chm| PDB=1chm | SCENE= }}
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'''ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES'''
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===ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES===
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==Overview==
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Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N(3) atom of the guanidinium group. OH- 377 adds to the C(1) atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site.
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(as it appears on PubMed at http://www.pubmed.gov), where 1696320 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1696320}}
==About this Structure==
==About this Structure==
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[[Category: Schumacher, G.]]
[[Category: Schumacher, G.]]
[[Category: Creatinase]]
[[Category: Creatinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:45:25 2008''

Revision as of 17:45, 30 June 2008

Image:1chm.png

Template:STRUCTURE 1chm

ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES

Template:ABSTRACT PUBMED 1696320

About this Structure

1CHM is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures., Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Russmann L, Schumacher G, J Mol Biol. 1990 Jul 20;214(2):597-610. PMID:1696320

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